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Volumn 80, Issue 9, 2014, Pages 2867-2873

Phasin proteins activate aeromonas caviae polyhydroxyalkanoate (PHA) synthase but not ralstonia eutropha PHA synthase

Author keywords

[No Author keywords available]

Indexed keywords

ASSAYS; ESCHERICHIA COLI; POLYMERIZATION; PROTEINS; SYNTHESIS (CHEMICAL);

EID: 84898636218     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.04179-13     Document Type: Article
Times cited : (39)

References (30)
  • 1
    • 0345688125 scopus 로고    scopus 로고
    • Polyester synthases: natural catalysts for plastics
    • Rehm BHA. 2003. Polyester synthases: natural catalysts for plastics. Biochem. J. 376:15-33. http://dx.doi.org/10.1042/BJ20031254.
    • (2003) Biochem. J , vol.376 , pp. 15-33
    • Rehm, B.H.A.1
  • 2
    • 0034501647 scopus 로고    scopus 로고
    • Synthesis, structure and properties of polyhydroxyalkanoates: biological polyesters
    • Sudesh K, Abe H, Doi Y. 2000. Synthesis, structure and properties of polyhydroxyalkanoates: biological polyesters. Prog. Polym. Sci. 25:1503-1555. http://dx.doi.org/10.1016/S0079-6700(00)00035-6.
    • (2000) Prog. Polym. Sci , vol.25 , pp. 1503-1555
    • Sudesh, K.1    Abe, H.2    Doi, Y.3
  • 3
    • 0842330739 scopus 로고    scopus 로고
    • An extra large insertion in the polyhydroxyalkanoate synthase from Delftia acidovorans DS-17: its deletion effects and relation to cellular proteolysis
    • Tsuge T, Imazu S, Takase K, Taguchi S, Doi Y. 2004. An extra large insertion in the polyhydroxyalkanoate synthase from Delftia acidovorans DS-17: its deletion effects and relation to cellular proteolysis. FEMS Microbiol. Lett. 231:77-83. http://dx.doi.org/10.1016/S0378-1097(03)00930-3.
    • (2004) FEMS Microbiol. Lett , vol.231 , pp. 77-83
    • Tsuge, T.1    Imazu, S.2    Takase, K.3    Taguchi, S.4    Doi, Y.5
  • 4
    • 0029039870 scopus 로고
    • Analysis of a 24-kilodalton protein associated with the polyhydroxyalkanoic acid granules in Alcaligenes eutrophus
    • Wieczorek R, Pries A, Steinbüchel A, Mayer F. 1995. Analysis of a 24-kilodalton protein associated with the polyhydroxyalkanoic acid granules in Alcaligenes eutrophus. J. Bacteriol. 177:2425-2435.
    • (1995) J. Bacteriol , vol.177 , pp. 2425-2435
    • Wieczorek, R.1    Pries, A.2    Steinbüchel, A.3    Mayer, F.4
  • 5
    • 0032974252 scopus 로고    scopus 로고
    • Re-evaluation of the primary structure of Ralstonia eutropha phasin and implications for polyhydroxyalkanoic acid granule binding
    • Hanleya SZ, Pappin DJC, Rahman D, White AJ, Elborough KM, Slabas AR. 1999. Re-evaluation of the primary structure of Ralstonia eutropha phasin and implications for polyhydroxyalkanoic acid granule binding. FEBS Lett. 447:99-105. http://dx.doi.org/10.1016/S0014-5793(99)00235-5.
    • (1999) FEBS Lett , vol.447 , pp. 99-105
    • Hanleya, S.Z.1    Pappin, D.J.C.2    Rahman, D.3    White, A.J.4    Elborough, K.M.5    Slabas, A.R.6
  • 6
    • 22244459223 scopus 로고    scopus 로고
    • Nontemplate-dependent polymerization processes: polyhydroxyalkanoate synthases as a paradigm
    • Stubbe J, Tian J, He A, Sinskey AJ, Lawrence AG, Liu P. 2005. Nontemplate-dependent polymerization processes: polyhydroxyalkanoate synthases as a paradigm. Annu. Rev. Biochem. 74:433-480. http://dx.doi.org/10.1146/annurev.biochem.74.082803.133013.
    • (2005) Annu. Rev. Biochem , vol.74 , pp. 433-480
    • Stubbe, J.1    Tian, J.2    He, A.3    Sinskey, A.J.4    Lawrence, A.G.5    Liu, P.6
  • 7
    • 0030802446 scopus 로고    scopus 로고
    • Cloning and analysis of the poly(3-hydroxybutyrate-co-3-hydroxyhexanoate) biosynthesis genes of Aeromonas caviae
    • Fukui T, Doi Y. 1997. Cloning and analysis of the poly(3-hydroxybutyrate-co-3-hydroxyhexanoate) biosynthesis genes of Aeromonas caviae. J. Bacteriol. 179:4821-4830.
    • (1997) J. Bacteriol , vol.179 , pp. 4821-4830
    • Fukui, T.1    Doi, Y.2
  • 8
    • 0033004435 scopus 로고    scopus 로고
    • Biosynthesis of polyhydroxyalkanoates (PHA) by recombinant Ralstonia eutropha and effects of PHA synthase activity on in vivo PHA biosynthesis
    • Kichise T, Fukui T, Yoshida Y, Doi Y. 1999. Biosynthesis of polyhydroxyalkanoates (PHA) by recombinant Ralstonia eutropha and effects of PHA synthase activity on in vivo PHA biosynthesis. Int. J. Biol. Macromol. 25:69-77. http://dx.doi.org/10.1016/S0141-8130(99)00017-3.
    • (1999) Int. J. Biol. Macromol , vol.25 , pp. 69-77
    • Kichise, T.1    Fukui, T.2    Yoshida, Y.3    Doi, Y.4
  • 9
    • 0034891510 scopus 로고    scopus 로고
    • Characterization of 13 kDa granule-associated protein in Aeromonas caviae and biosynthesis of polyhydroxyalkanoates with altered molar composition by recombinant bacteria
    • Fukui T, Kichise T, Iwata T, Doi Y. 2001. Characterization of 13 kDa granule-associated protein in Aeromonas caviae and biosynthesis of polyhydroxyalkanoates with altered molar composition by recombinant bacteria. Biomacromolecules 2:148-153. http://dx.doi.org/10.1021/bm005 6052.
    • (2001) Biomacromolecules , vol.2 , pp. 148-153
    • Fukui, T.1    Kichise, T.2    Iwata, T.3    Doi, Y.4
  • 10
    • 13844318652 scopus 로고    scopus 로고
    • Effect of overexpression of phasin gene from Aeromonas hydrophila on biosynthesis of copolyesters of 3-hydroxybutyrate and 3-hydroxyhexanoate
    • Tian SJ, Lai WJ, Zheng Z, Wang HX, Chen GQ. 2005. Effect of overexpression of phasin gene from Aeromonas hydrophila on biosynthesis of copolyesters of 3-hydroxybutyrate and 3-hydroxyhexanoate. FEMS Microbiol. Lett. 244:19-25. http://dx.doi.org/10.1016/j.femsle.2005.01.020.
    • (2005) FEMS Microbiol. Lett , vol.244 , pp. 19-25
    • Tian, S.J.1    Lai, W.J.2    Zheng, Z.3    Wang, H.X.4    Chen, G.Q.5
  • 11
    • 84857689288 scopus 로고    scopus 로고
    • Development and validation of an HPLC-based screening method to acquire polyhydroxyalkanoate synthase mutants with altered substrate specificity
    • Watanabe Y, Ichinomiya Y, Shimada D, Saika A, Abe H, Taguchi S, Tsuge T. 2012. Development and validation of an HPLC-based screening method to acquire polyhydroxyalkanoate synthase mutants with altered substrate specificity. J. Biosci. Bioeng. 113:286-292. http://dx.doi.org/10.1016/j.jbiosc.2011.10.015.
    • (2012) J. Biosci. Bioeng , vol.113 , pp. 286-292
    • Watanabe, Y.1    Ichinomiya, Y.2    Shimada, D.3    Saika, A.4    Abe, H.5    Taguchi, S.6    Tsuge, T.7
  • 12
    • 0034014195 scopus 로고    scopus 로고
    • Biosynthesis of poly(3-hydroxybutyrate-co-3-hydroxyalkanoates) by recombinant bacteria expressing the PHA synthase gene phaC1 from Pseudomonas sp
    • Matsusaki H, Abe H, Taguchi T, Fukui T, Doi Y. 2000. Biosynthesis of poly(3-hydroxybutyrate-co-3-hydroxyalkanoates) by recombinant bacteria expressing the PHA synthase gene phaC1 from Pseudomonas sp. 61-3. Appl. Microbiol. Biotechnol. 53:401-409. http://dx.doi.org/10.1007/s0025 30051633.
    • (2000) 61-3. Appl. Microbiol. Biotechnol , vol.53 , pp. 401-409
    • Matsusaki, H.1    Abe, H.2    Taguchi, T.3    Fukui, T.4    Doi, Y.5
  • 13
    • 31444453669 scopus 로고    scopus 로고
    • Molecular weight characterization of poly[(R)-3-hydroxybutyrate] synthesized by genetically engineered strains of Escherichia coli
    • Agus J, Kahar P, Abe H, Doi Y, Tsuge T. 2006. Molecular weight characterization of poly[(R)-3-hydroxybutyrate] synthesized by genetically engineered strains of Escherichia coli. Polym. Degrad. Stab. 91:1138-1146. http://dx.doi.org/10.1016/j.polymdegradstab.2005.07.006.
    • (2006) Polym. Degrad. Stab , vol.91 , pp. 1138-1146
    • Agus, J.1    Kahar, P.2    Abe, H.3    Doi, Y.4    Tsuge, T.5
  • 14
    • 0028793123 scopus 로고
    • Four new derivatives of the broad-host-range cloning vector pBBR1MCS, carrying different antibiotic-resistance cassettes
    • Kovach ME, Elzer PH, Hill DS, Robertson GT, Farris MA, Roop RM, II, Peterson KM. 1995. Four new derivatives of the broad-host-range cloning vector pBBR1MCS, carrying different antibiotic-resistance cassettes. Gene 166:175-176. http://dx.doi.org/10.1016/0378-1119(95)00584-1.
    • (1995) Gene , vol.166 , pp. 175-176
    • Kovach, M.E.1    Elzer, P.H.2    Hill, D.S.3    Robertson, G.T.4    Farris, M.A.5    Roop II, R.M.6    Peterson, K.M.7
  • 15
    • 84869053075 scopus 로고    scopus 로고
    • Active intermediates of polyhydroxyalkanoate synthase from Aeromonas caviae in polymerization reaction
    • Numata K, Motoda Y, Watanabe S, Tochio N, Kigawa T, Doi Y. 2012. Active intermediates of polyhydroxyalkanoate synthase from Aeromonas caviae in polymerization reaction. Biomacromolecules 13:3450-3455. http://dx.doi.org/10.1021/bm301276k.
    • (2012) Biomacromolecules , vol.13 , pp. 3450-3455
    • Numata, K.1    Motoda, Y.2    Watanabe, S.3    Tochio, N.4    Kigawa, T.5    Doi, Y.6
  • 16
    • 20444497775 scopus 로고    scopus 로고
    • Characterization and properties of G4X mutants of Ralstonia eutropha PHA synthase for poly(3-hydroxybutyrate) biosynthesis in Escherichia coli
    • Normi YM, Hiraishi T, Taguchi S, Abe H, Sudesh K, Najimudin N, Doi Y. 2005. Characterization and properties of G4X mutants of Ralstonia eutropha PHA synthase for poly(3-hydroxybutyrate) biosynthesis in Escherichia coli. Macromol. Biosci. 5:197-206. http://dx.doi.org/10.1002/mabi.200400181.
    • (2005) Macromol. Biosci , vol.5 , pp. 197-206
    • Normi, Y.M.1    Hiraishi, T.2    Taguchi, S.3    Abe, H.4    Sudesh, K.5    Najimudin, N.6    Doi, Y.7
  • 17
    • 84876972140 scopus 로고    scopus 로고
    • Characterization of polyhydroxyalkanoate (PHA) synthase derived from Delftia acidovorans DS-17 and the influence of PHA production in Escherichia coli
    • Hiroe A, Ushimaru K, Tsuge T. 2013. Characterization of polyhydroxyalkanoate (PHA) synthase derived from Delftia acidovorans DS-17 and the influence of PHA production in Escherichia coli. J. Biosci. Bioeng. 115: 633-638. http://dx.doi.org/10.1016/j.jbiosc.2012.12.015.
    • (2013) J. Biosci. Bioeng , vol.115 , pp. 633-638
    • Hiroe, A.1    Ushimaru, K.2    Tsuge, T.3
  • 18
    • 84874104779 scopus 로고    scopus 로고
    • New insights into activation and substrate recognition of polyhydroxyalkanoate synthase from Ralstonia eutropha
    • Ushimaru K, Sangiambut S, Thomson N, Sivaniah E, Tsuge T. 2013. New insights into activation and substrate recognition of polyhydroxyalkanoate synthase from Ralstonia eutropha. Appl. Microbiol. Biotechnol. 97:1175-1182. http://dx.doi.org/10.1007/s00253-012-4089-x.
    • (2013) Appl. Microbiol. Biotechnol , vol.97 , pp. 1175-1182
    • Ushimaru, K.1    Sangiambut, S.2    Thomson, N.3    Sivaniah, E.4    Tsuge, T.5
  • 19
    • 55049090025 scopus 로고    scopus 로고
    • Polyhydroxyalkanoate film formation and synthase activity during in vitro and in situ polymerization on hydrophobic surfaces
    • Sato S, Ono Y, Mochiyama Y, Sivaniah E, Kikkawa Y, Sudesh K, Hiraishi T, Doi Y, Abe H, Tsuge T. 2008. Polyhydroxyalkanoate film formation and synthase activity during in vitro and in situ polymerization on hydrophobic surfaces. Biomacromolecules 9:2811-2818. http://dx.doi.org/10.1021/bm800566s.
    • (2008) Biomacromolecules , vol.9 , pp. 2811-2818
    • Sato, S.1    Ono, Y.2    Mochiyama, Y.3    Sivaniah, E.4    Kikkawa, Y.5    Sudesh, K.6    Hiraishi, T.7    Doi, Y.8    Abe, H.9    Tsuge, T.10
  • 21
    • 0029899079 scopus 로고    scopus 로고
    • Production of a novel copolyester of 3-hydroxybutyric acid and medium-chain-length 3-hydroxyalkanoic acids by Pseudomonas sp. 61-3 from sugars
    • Kato M, Bao HJ, Kang CK, Fukui T, Doi Y. 1996. Production of a novel copolyester of 3-hydroxybutyric acid and medium-chain-length 3-hydroxyalkanoic acids by Pseudomonas sp. 61-3 from sugars. Appl. Microbiol. Biotechnol. 45:363-370. http://dx.doi.org/10.1007/s002530050697.
    • (1996) Appl. Microbiol. Biotechnol , vol.45 , pp. 363-370
    • Kato, M.1    Bao, H.J.2    Kang, C.K.3    Fukui, T.4    Doi, Y.5
  • 22
    • 0032922774 scopus 로고    scopus 로고
    • Co-expression of polyhydroxyalkanoate synthase and (R)-enoyl-CoA hydratase genes of Aeromonas caviae establishes copolyester biosynthesis pathway in Escherichia coli
    • Fukui T, Yokomizo S, Kobayashi G, Doi Y. 1999. Co-expression of polyhydroxyalkanoate synthase and (R)-enoyl-CoA hydratase genes of Aeromonas caviae establishes copolyester biosynthesis pathway in Escherichia coli. FEMS Microbiol. Lett. 170:69-75. http://dx.doi.org/10.1111/j.1574-6968.1999.tb13356.x.
    • (1999) FEMS Microbiol. Lett , vol.170 , pp. 69-75
    • Fukui, T.1    Yokomizo, S.2    Kobayashi, G.3    Doi, Y.4
  • 23
    • 84861112411 scopus 로고    scopus 로고
    • Rearrangement of gene order in the phaCAB operon leads to effective production of ultrahigh-molecular-weight poly[(R)-3-hydroxybutyrate] in genetically engineered Escherichia coli
    • Hiroe A, Tsuge K, Nomura CT, Itaya M, Tsuge T. 2012. Rearrangement of gene order in the phaCAB operon leads to effective production of ultrahigh-molecular-weight poly[(R)-3-hydroxybutyrate] in genetically engineered Escherichia coli. Appl. Environ. Microbiol. 78:3177-3184. http://dx.doi.org/10.1128/AEM.07715-11.
    • (2012) Appl. Environ. Microbiol , vol.78 , pp. 3177-3184
    • Hiroe, A.1    Tsuge, K.2    Nomura, C.T.3    Itaya, M.4    Tsuge, T.5
  • 24
    • 0035078527 scopus 로고    scopus 로고
    • New insight into the role of the PhaP phasin of Ralstonia eutropha in promoting synthesis of polyhydroxybutyrate
    • York GM, Stubbe JA, Sinskey AJ. 2001. New insight into the role of the PhaP phasin of Ralstonia eutropha in promoting synthesis of polyhydroxybutyrate. J. Bacteriol. 183:2394-2397. http://dx.doi.org/10.1128/JB.183.7.2394-2397.2001.
    • (2001) J. Bacteriol , vol.183 , pp. 2394-2397
    • York, G.M.1    Stubbe, J.A.2    Sinskey, A.J.3
  • 25
    • 0036136119 scopus 로고    scopus 로고
    • The Ralstonia eutropha PhaR protein couples synthesis of the PhaP phasin to the presence of polyhydroxybutyrate in cells and promotes polyhydroxybutyrate production
    • York GM, Stubbe JA, Sinskey AJ. 2002. The Ralstonia eutropha PhaR protein couples synthesis of the PhaP phasin to the presence of polyhydroxybutyrate in cells and promotes polyhydroxybutyrate production. J. Bacteriol. 184:59-66. http://dx.doi.org/10.1128/JB.184.1.59-66.2002.
    • (2002) J. Bacteriol , vol.184 , pp. 59-66
    • York, G.M.1    Stubbe, J.A.2    Sinskey, A.J.3
  • 26
    • 84892460614 scopus 로고    scopus 로고
    • PhaM is the physiological activator of PHB synthase (PhaC1) in Ralstonia eutropha
    • Pfeiffer D, Jendrossek D. 2013. PhaM is the physiological activator of PHB synthase (PhaC1) in Ralstonia eutropha. Appl. Environ. Microbiol. http://dx.doi.org/10.1128/AEM.02935-13.
    • (2013) Appl. Environ. Microbiol
    • Pfeiffer, D.1    Jendrossek, D.2
  • 27
    • 84858680303 scopus 로고    scopus 로고
    • Purification of polyhydroxybutyrate synthase from its native organism, Ralstonia eutropha: implications for the initiation and elongation of polymer formation in vivo
    • Cho M, Brigham CJ, Sinskey AJ, Stubbe J. 2012. Purification of polyhydroxybutyrate synthase from its native organism, Ralstonia eutropha: implications for the initiation and elongation of polymer formation in vivo. Biochemistry 51:2276-2288. http://dx.doi.org/10.1021/bi2013596.
    • (2012) Biochemistry , vol.51 , pp. 2276-2288
    • Cho, M.1    Brigham, C.J.2    Sinskey, A.J.3    Stubbe, J.4
  • 28
    • 41949101592 scopus 로고    scopus 로고
    • Binding of the major phasin, PhaP1, from Ralstonia eutropha H16 to poly(3-hydroxybutyrate) granules
    • Neumann L, Spinozzi F, Sinibaldi R, Rustichelli F, Pötter M, Steinbüchel A. 2008. Binding of the major phasin, PhaP1, from Ralstonia eutropha H16 to poly(3-hydroxybutyrate) granules. J. Bacteriol. 190: 2911-2919. http://dx.doi.org/10.1128/JB.01486-07.
    • (2008) J. Bacteriol , vol.190 , pp. 2911-2919
    • Neumann, L.1    Spinozzi, F.2    Sinibaldi, R.3    Rustichelli, F.4    Pötter, M.5    Steinbüchel, A.6
  • 29
    • 33747167624 scopus 로고    scopus 로고
    • Crystallization and initial X-ray analysis of polyhydroxyalkanoate granule-associated protein from Aeromonas hydrophila
    • Zhao M, Li Z, Zheng W, Lou Z, Chen GQ. 2006. Crystallization and initial X-ray analysis of polyhydroxyalkanoate granule-associated protein from Aeromonas hydrophila. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 62:814-819. http://dx.doi.org/10.1107/S1744309106025000.
    • (2006) Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun , vol.62 , pp. 814-819
    • Zhao, M.1    Li, Z.2    Zheng, W.3    Lou, Z.4    Chen, G.Q.5
  • 30
    • 27544449176 scopus 로고    scopus 로고
    • Organization of polyhydroxyalkanoate synthase for in vitro polymerization as revealed by atomic force microscopy
    • Kikkawa Y, Narike M, Hiraishi T, Kanesato M, Sudesh K, Doi Y, Tsuge T. 2005. Organization of polyhydroxyalkanoate synthase for in vitro polymerization as revealed by atomic force microscopy. Macromol. Biosci. 5:929-935. http://dx.doi.org/10.1002/mabi.200500115.
    • (2005) Macromol. Biosci , vol.5 , pp. 929-935
    • Kikkawa, Y.1    Narike, M.2    Hiraishi, T.3    Kanesato, M.4    Sudesh, K.5    Doi, Y.6    Tsuge, T.7


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